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Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins

Published on: May 30, 2025

Novel eukaryotic enzymes modifying cell-surface biopolymers.

Vivek Anantharaman¹, L Aravind

¹National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA.

|January 9, 2010

Summary

This summary is machine-generated.

Novel enzymes identified modify eukaryotic cell surface glycans, impacting properties like strength and host-pathogen interactions. These findings are crucial for understanding plant and animal biology.

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Area of Science:

Biochemistry
Molecular Biology
Genomics

Background:

Eukaryotic extracellular matrices comprise modified proteins, glycans, and biopolymers.
Comparative genomics and sequence analysis reveal novel enzymes for cell-surface glycan/glycoprotein modification.

Purpose of the Study:

To identify and characterize novel enzymes involved in eukaryotic extracellular matrix modification.
To elucidate the functional roles of these enzymes in biological processes.

Main Methods:

Comparative genomics and sequence profile analysis.
Identification and characterization of enzyme domains (acyltransferase, esterase).
Analysis of enzyme conservation patterns.

Main Results:

Defined the acyltransferase domain (fungal Cas1p) and unified it with classical 10TM acyltransferases.
Identified a novel esterase family (N-terminal domain of Cas1p) with distinct conservation from SGNH/GDSL esterases.
Uncovered fused esterase-ligase enzymes in metazoans.

Conclusions:

The combined action of acyltransferase and esterase domains regulates glycan acylation, affecting physical properties and host-pathogen interactions.
These enzymes are implicated in plant transpiration and stress resistance (e.g., PMR5, ESK1).
Metazoan esterases may modify cell surface polymers with amino acids or peptides.